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Copper in PDB 5zpt: Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2)

Enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2)

All present enzymatic activity of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2):
1.4.3.21;

Protein crystallography data

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2), PDB code: 5zpt was solved by T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, K.Tanizawa, T.Kumasaka, M.Yamamoto, T.Okajima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.63 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 193.269, 64.850, 159.119, 90.00, 117.10, 90.00
R / Rfree (%) 16.2 / 19.4

Other elements in 5zpt:

The structure of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2) also contains other interesting chemical elements:

Sodium (Na) 3 atoms

Copper Binding Sites:

The binding sites of Copper atom in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2) (pdb code 5zpt). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2), PDB code: 5zpt:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 5zpt

Go back to Copper Binding Sites List in 5zpt
Copper binding site 1 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu701

b:11.2
occ:1.00
O A:HOH817 1.9 27.7 1.0
ND1 A:HIS592 2.0 12.9 1.0
NE2 A:HIS431 2.0 8.3 1.0
NE2 A:HIS433 2.1 8.2 1.0
OH A:TYQ382 2.7 16.9 1.0
CD2 A:HIS433 2.9 7.3 1.0
CE1 A:HIS431 3.0 9.3 1.0
CG A:HIS592 3.0 10.8 1.0
CE1 A:HIS592 3.0 14.9 1.0
CD2 A:HIS431 3.0 6.9 1.0
CE1 A:HIS433 3.2 7.2 1.0
CB A:HIS592 3.3 8.8 1.0
CZ A:TYQ382 3.6 25.4 1.0
N5 A:TYQ382 4.1 30.9 1.0
ND1 A:HIS431 4.1 5.5 1.0
NE2 A:HIS592 4.1 12.6 1.0
CG A:HIS433 4.1 11.4 1.0
CD2 A:HIS592 4.1 12.5 1.0
CG A:HIS431 4.2 9.1 1.0
CE2 A:TYQ382 4.2 25.3 1.0
ND1 A:HIS433 4.2 8.1 1.0
CE1 A:TYQ382 4.4 23.0 1.0
O A:HOH904 4.4 11.3 1.0
CA A:HIS592 4.8 9.3 1.0
SD A:MET602 4.9 23.3 1.0

Copper binding site 2 out of 2 in 5zpt

Go back to Copper Binding Sites List in 5zpt
Copper binding site 2 out of 2 in the Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Copper Amine Oxidase From Arthrobacter Globiformis Anaerobically Reduced By Phenylethylamine at pH 10 at 288 K (2) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu701

b:14.8
occ:1.00
NE2 B:HIS431 2.0 8.7 1.0
NE2 B:HIS433 2.1 8.6 1.0
O B:HOH810 2.1 33.4 1.0
ND1 B:HIS592 2.1 17.7 1.0
OH B:TYQ382 2.6 18.7 1.0
CD2 B:HIS431 3.0 6.8 1.0
CD2 B:HIS433 3.0 7.0 1.0
CE1 B:HIS431 3.0 8.8 1.0
CE1 B:HIS592 3.1 13.3 1.0
CG B:HIS592 3.1 13.2 1.0
CE1 B:HIS433 3.1 12.3 1.0
CB B:HIS592 3.4 7.9 1.0
CZ B:TYQ382 3.4 24.7 1.0
O B:HOH1235 3.5 44.3 1.0
N5 B:TYQ382 3.7 42.9 1.0
CE2 B:TYQ382 3.9 30.5 1.0
ND1 B:HIS431 4.1 7.2 1.0
CG B:HIS431 4.1 7.9 1.0
CG B:HIS433 4.2 11.2 1.0
NE2 B:HIS592 4.2 10.8 1.0
ND1 B:HIS433 4.2 9.9 1.0
CD2 B:HIS592 4.2 12.3 1.0
CE1 B:TYQ382 4.4 24.7 1.0
O B:HOH842 4.4 17.2 1.0
CG2 B:VAL406 4.6 17.5 0.4
CA B:HIS592 4.9 10.9 1.0
SD B:MET602 5.0 21.6 1.0

Reference:

T.Murakawa, S.Baba, Y.Kawano, H.Hayashi, T.Yano, T.Kumasaka, M.Yamamoto, K.Tanizawa, T.Okajima. In Crystallothermodynamic Analysis of Conformational Change of the Topaquinone Cofactor in Bacterial Copper Amine Oxidase. Proc. Natl. Acad. Sci. V. 116 135 2019U.S.A..
ISSN: ESSN 1091-6490
PubMed: 30563857
DOI: 10.1073/PNAS.1811837116
Page generated: Mon Jul 14 05:52:19 2025

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